ACSL1 (human, recombinant; aa 48-698)

Acyl-CoA synthetase long-chain family member 1 (ACSL1) is a long-chain acyl-CoA synthase that converts both saturated and unsaturated fatty acids into fatty acyl-CoA esters.^1,2,3 It is expressed in liver, heart, adipose tissue, and muscle and, in the presence of TANK-binding kinase 1 (TBK1), localizes to the mitochondria where it promotes fatty acid β-oxidation.^4,5 In the absence of TBK1, ACSL1 is localized to the endoplasmic reticulum (ER) and facilitates lipid accumulation.⁴ ACSL1 has broad substrate specificity for 16- and 18-carbon saturated fatty acids and 16-20-carbon unsaturated fatty acids.⁵ ACSL1 knockdown suppresses palmitate-induced increases in the inflammatory markers TNF-α, IL-1β, and CD11c and inhibits lipid accumulation and the transition into foam cells in THP-1 macrophages, as well as inhibits ferroptosis induced by α-eleostearic acid (9(Z),11(E),13(E)-octadecatrienoic acid (Item No. 10008349) in BT-549 cells.^6,7 Levels of ACSL1 are increased in liver, breast, ovarian, and colorectal cancers compared with non-cancerous tissues.¹ Cayman’s ACSL1 (human, recombinant; aa 48-698) protein can be used for ELISA, enzyme activity, and Western blot (WB) applications.

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1. Quan, J., Bode, A.M., and Luo, X. ACSL family: The regulatory mechanisms and therapeutic implications in cancer. Eur. J. Pharmacol. 909, 174397 (2021).

2. Tsushima, K., Bugger, H., Wende, A.R., et al. Mitochondrial reactive oxygen species in lipotoxic hearts induce post-translational modifications of AKAP121, DRP1, and OPA1 that promote mitochondrial fission. Circ. Res. 122(1), 58-73 (2018).

3. Zhao, L., Pascual, F., Bacudio, L., et al. Defective fatty acid oxidation in mice with muscle-specific acyl-CoA synthetase 1 deficiency increases amino acid use and impairs muscle function. The Journal of Biological Chemisty 294(22), 8819-8833 (2019).

4. Huh, J.Y., Reilly, S.M., Abu-Odeh, M., et al. TANK-binding kinase 1 regulates the localization of acyl-CoA synthetase ACSL1 to control hepatic fatty acid oxidation. Cell Metab. 32(6), 1012-1027 (2020).

5. Singh, A.B., Dong, B., Xu, Y., et al. Identification of a novel function of hepatic long-chain acyl-CoA synthetase-1 (ACSL1) in bile acid synthesis and its regulation by bile acid-activated farnesoid X receptor. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864(3), 358-371 (2019).

6. Al-Rashed, F., Haddad, D., Al Madhoun, A., et al. ACSL1 is a key regulator of inflammatory and macrophage foaming induced by short-term palmitate exposure or acute high-fat feeding. iScience 26(7), 107145 (2023).

7. Beatty, A., Singh, T., Tyurina, Y.Y., et al. Ferroptotic cell death triggered by conjugated linolenic acids is mediated by ACSL1. Nat. Commun. 12(1), 2244 (2021).